1vla

Crystal structure of Hydroperoxide resistance protein OsmC (TM0919) from Thermotoga maritima at 1.80 A resolution

Method: X-RAY DIFFRACTION

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Hydroperoxide resistance protein OsmC

Thermotoga maritima

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9X021_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 13–150； UniProt 1–138 Author chain B； PDBConstruct 13–150； UniProt 1–138 Author chain C； PDBConstruct 13–150； UniProt 1–138 Author chain D； PDBConstruct 13–150； UniProt 1–138

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1vla
Deposition date deposition_date	2004-07-15
Structure title title	Crystal structure of Hydroperoxide resistance protein OsmC (TM0919) from Thermotoga maritima at 1.80 A resolution
Keywords keywords	;TM0919, HYDROPEROXIDE RESISTANCE PROTEIN OSMC, STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI, Joint Center for Structural Genomics, OXIDOREDUCTASE ;; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1vla__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1vla__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1vla__assembly_2__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	20.06 Å
Rg (electron density)	19.45 Å
Total Rg	20.03 Å
Atom count	2164
Residues	261
Excluded volume	39058 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1vla__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1vla__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1vla__assembly_3__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (7 domains)

Domain ID domain_id	d1vlaa1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.227 — OsmC-like
Superfamily Superfamily superfamily	d.227.1 — OsmC-like
Family Family family	d.227.1.2 — YhfA-like

Domain ID domain_id	d1vlaa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1vlab1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.227 — OsmC-like
Superfamily Superfamily superfamily	d.227.1 — OsmC-like
Family Family family	d.227.1.2 — YhfA-like

Domain ID domain_id	d1vlab2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1vlac1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.227 — OsmC-like
Superfamily Superfamily superfamily	d.227.1 — OsmC-like
Family Family family	d.227.1.2 — YhfA-like

Domain ID domain_id	d1vlac2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1vlad_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.227 — OsmC-like
Superfamily Superfamily superfamily	d.227.1 — OsmC-like
Family Family family	d.227.1.2 — YhfA-like

CATH v4.4 (8 domains)

Domain ID domain_id	1vlaA01
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	25 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1vlaA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	20 — K homology (KH) domain

Domain ID domain_id	1vlaB01
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	25 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1vlaB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	20 — K homology (KH) domain

Domain ID domain_id	1vlaC01
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	25 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1vlaC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	20 — K homology (KH) domain

Domain ID domain_id	1vlaD01
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	25 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1vlaD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	20 — K homology (KH) domain

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Unit-cell length a length_a	64.754 Å
Unit-cell length b length_b	39.789 Å
Unit-cell length c length_c	110.448 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	93.79 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	29.320 Å
R factor r_factor	0.1729
R_work r_work	0.1703
R_free r_free	0.2213

Description description	Hydroperoxide resistance protein OsmC
Molecular weight formula_weight	17912.4 kDa
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	4999

Crystal structure of Hydroperoxide resistance protein OsmC (TM0919) from Thermotoga maritima at 1.80 A resolution

1. Protein Identity and Related Structures Protein Identity & Related Structures

Hydroperoxide resistance protein OsmC

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1vla__assembly_2__model_1

1vla__assembly_2__model_1 | I(q)

1vla__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (7 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Source organism organism	Thermotoga maritima
NCBI taxonomy ID ncbi_taxonomy_id	243274
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	464

Crystal structure of Hydroperoxide resistance protein OsmC (TM0919) from Thermotoga maritima at 1.80 A resolution

1. Protein Identity and Related Structures Protein Identity & Related Structures

Hydroperoxide resistance protein OsmC

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1vla__assembly_2__model_1

1vla__assembly_2__model_1 | I(q)

1vla__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (7 domains)

CATH v4.4 (8 domains)

7. Citations (1)